By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Proteins have been published. According to news reporting from Bochum, Germany, by NewsRx journalists, research stated, "In anaerobiosis, the green alga Chlamydomonas reinhardtii evolves molecular hydrogen (H(2)) as one of several fermentation products. H(2) is generated mostly by the [Fe-Fe]-hydrogenase HYDA1, which uses plant type ferredoxin PETF/FDX1 (PETF) as an electron donor."
The news correspondents obtained a quote from the research from Ruhr University, "Dark fermentation of the alga is mainly of the mixed acid type, because formate, ethanol, and acetate are generated by a pyruvate:formate lyase pathway similar to Escherichia coli. However, C. reinhardtii also possesses the pyruvate:ferredoxin oxidoreductase PFR1, which, like pyruvate:formate lyase and HYDA1, is localized in the chloroplast. PFR1 has long been suggested to be responsible for the low but significant H(2) accumulation in the dark because the catalytic mechanism of pyruvate:ferredoxin oxidoreductase involves the reduction of ferredoxin. With the aim of proving the biochemical feasibility of the postulated reaction, we have heterologously expressed the PFR1 gene in E. coli. Purified recombinant PFR1 is able to transfer electrons from pyruvate to HYDA1, using the ferredoxins PETF and FDX2 as electron carriers. The high reactivity of PFR1 toward oxaloacetate indicates that in vivo, fermentation might also be coupled to an anaerobically active glyoxylate cycle."
According to the news reporters, the research concluded: "Our results suggest that C. reinhardtii employs a clostridial type H(2) production pathway in the dark, especially because C. reinhardtii PFR1 was also able to allow H(2) evolution in reaction mixtures containing Clostridium acetobutylicum 2[4Fe-4S]-ferredoxin and [Fe-Fe]-hydrogenase HYDA."
For more information on this research see: Pyruvate:ferredoxin oxidoreductase is coupled to light-independent hydrogen production in Chlamydomonas reinhardtii. Journal of Biological Chemistry, 2013;288(6):4368-77. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
Our news journalists report that additional information may be obtained by contacting J. Noth, Ruhr Universitat Bochum, Fakultat fur Biologie und Biotechnologie, AG Photobiotechnologie, 44801 Bochum, Germany. Additional authors for this research include D. Krawietz, A. Hemschemeier and T. Happe (see also Proteins).
Keywords for this news article include: Gases, Bochum, Europe, Germany, Elements, Hydrogen, Pyruvates, Keto Acids, Ferredoxins, Plant Proteins, Metalloproteins, Oxidoreductases, Carrier Proteins, Bacterial Proteins, Inorganic Chemicals, Iron Sulfur Proteins, Enzymes and Coenzymes, Iron Binding Proteins.
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